IndraLab

Statements

Phosphatidylinositol phosphate binds KCNQ1. 21 / 21
| 8 13
reach
"These characterizations support an agonistic role of PIP 2 binding for channel activation.Compared to the closed structure of PIP 2 -free KCNQ1, binding of PIP 2 within the VSD of KCNQ4 results in rea[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
33238160
sparser
"Superimposing the KCNQ2 structure ( xref ) with the homologous structure of KCNQ1 bound to PIP 2(55) ( xref ), we noted that residue R214 lies very close to PIP 2 , suggesting that R214 in the KCNQ2 channel could form part of the positively charged pocket that coordinates PIP 2 binding ( xref )."
35642783
reach
"Also, the mode of PIP 2 interaction with KCNQ1 remains elusive."
24721657
sparser
"Thus, for R366Q and R555C mutant channels, regulation of the channel by PIP 2 was potentiated, suggesting that PKA and PKC activate the channel by strengthening KCNQ1 interactions with PIP 2 ."
22787448
sparser
"Mechanisms that cause LOF in variants exhibiting intact cell surface expression include: deleterious effects on ion conduction, altered voltage sensitivity, disrupted KCNQ1-KCNE1, KCNQ1-calmodulin, or KCNQ1-PIP 2 interactions, or altered rate/capacity to undergo the conformational changes required for channel opening ( xref )."
39969993
sparser
"Also, the mode of PIP 2 interaction with KCNQ1 remains elusive."
24721657
reach
"Superimposing the KCNQ2 structure (Long et al., 2005) with the homologous structure of KCNQ1 bound to PIP (Figure 5—figure supplement 2B), we noted that residue R214 lies very close to PIP , suggesting that R214 in the KCNQ2 channel could form part of the positively charged pocket that coordinates PIP binding (Figure 5—figure supplement 2B)."
35642783
sparser
"We previously identified a cluster of basic residues in the proximal C-terminus of KCNQ1 that form a PIP 2 /phosphoinositide binding site."
29020060
reach
"Some LQTS associated mutations (R539W and R555C) might weaken the interaction between KCNQ1 and KCNE1 and PIP 2 and therefore destabilize the PIP 2 -mediated open state of KCNQ1 and KCNE1 channels [XREF_BIBR]."
33322401
sparser
"It is thought that increases in cytosolic Ca 2+ can compensate for receptor-mediated depletion of PIP 2 via an interaction between the calcified N lobe of CaM and the KCNQ1 proximal C-terminus (at Helix B) that mimics or substitutes for the KCNQ1-PIP 2 interaction to curtail I Ks current inhibition ( xref )."
32655402
reach
"Voltage-Dependent Regulation of PIP 2 Binding in KCNQ1.."
37192161
sparser
"But in HsKCNQ1-CaM ML277-PIP2-B, due to the release of CaM from VSD in the structural rearrangements, PIP 2 –I only interacts with KCNQ1."
37976835
reach
"It is not yet known whether KCNE3 has similar effects, but all members of the KCNE family possess similar residues to those important for modifying the manner in which PIP 2 interacts with KCNQ1 60."
26410412
sparser
"Among all lipids, four PIP 2 molecules interacted with several positive residues of Kv7.1 simultaneously, consistent with strong binding of PIP 2 to the channel."
25559286
reach
"As a result, both novel structures and states have been observed, with many cryo-EM structures of membrane proteins revealing lipids, including phosphatidylglycerol (PG), cholesterol, PIP and phosphatidylinositol (PI), bound to the structures.10Recent cryo-EM structures of the KCNQ1 and K 3.2 channels have captured binding sites for PIP ."
34139216
sparser
"Some Long QT mutations of KCNQ1, including R243H, R539W and R555C have been shown to decrease KCNQ1 interaction with PIP 2 ."
24681627
sparser
"Regarding KCNQ1, we have shown that type 1 long QT (LQT1) syndrome can be associated with a decrease in KCNQ1-PIP 2 interactions provoked by mutations in the S4–S5 linker (R243H) and in the C-terminal domain CTD (R539W and R555C) xref ."
24681627
sparser
"Analyzing the average number of salt bridges for prolonged trajectories (additional 20 and 40 ns), we have found similar interactions between Kv7.1 and PIP 2 (see xref ), indicating that the performed simulations have converged within the 100 ns time scale."
25559286
reach
"Interestingly, it has been suggested that PIP and CaM binding sites within the Kv7 channels overlap (Delmas and Brown, 2005; Haitin and Attali, 2008), accordingly, binding of PIP and PIP to Kv7.1 have been shown to compete against CaM (Kwon et al., 2007)."
18971466
sparser
"Quercetin also docked to the top of the VSD in the cryo-EM-derived structure of human KCNQ1-PIP 2 -calmodulin/KCNE3 xref , notably being predicted to H-bond to the R231 sidechain."
32641720
sparser
"Out of 27 KCNQ1 predicted binding clusters in the KCNQ1-PIP 2 -calmodulin/KCNE3 structure, the top three in terms of most negative ΔG values (−8.75, −8.26 and −7.82 kJ/mol) positioned quercetin close to and/or H-binding with the R231 sidechain (Fig.  xref )."
32641720